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Q99497

- PARK7_HUMAN

UniProt

Q99497 - PARK7_HUMAN

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Protein

Protein DJ-1

Gene
PARK7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Protects cells against oxidative stress and cell death. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone. May regulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells.15 Publications

Kineticsi

  1. KM=173.4 µM for casein1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061 Inferred
Active sitei126 – 1261 Inferred

GO - Molecular functioni

  1. androgen receptor binding Source: ParkinsonsUK-UCL
  2. cytokine binding Source: ParkinsonsUK-UCL
  3. identical protein binding Source: ParkinsonsUK-UCL
  4. mRNA binding Source: UniProtKB
  5. peptidase activity Source: UniProtKB
  6. peroxidase activity Source: UniProtKB
  7. peroxiredoxin activity Source: Ensembl
  8. protein binding Source: UniProtKB
  9. protein homodimerization activity Source: UniProtKB
  10. receptor binding Source: UniProtKB
  11. scaffold protein binding Source: ParkinsonsUK-UCL
  12. small protein activating enzyme binding Source: ParkinsonsUK-UCL
  13. small protein conjugating enzyme binding Source: ParkinsonsUK-UCL
  14. transcription factor binding Source: ParkinsonsUK-UCL
  15. ubiquitin-specific protease binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. adult locomotory behavior Source: Ensembl
  2. autophagy Source: UniProtKB-KW
  3. cellular response to hydrogen peroxide Source: UniProtKB
  4. cellular response to oxidative stress Source: ParkinsonsUK-UCL
  5. dopamine uptake involved in synaptic transmission Source: Ensembl
  6. hydrogen peroxide metabolic process Source: Ensembl
  7. inflammatory response Source: UniProtKB-KW
  8. membrane depolarization Source: Ensembl
  9. membrane hyperpolarization Source: Ensembl
  10. mitochondrion organization Source: UniProtKB
  11. negative regulation of cell death Source: UniProtKB
  12. negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: ParkinsonsUK-UCL
  13. negative regulation of death-inducing signaling complex assembly Source: ParkinsonsUK-UCL
  14. negative regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  15. negative regulation of neuron apoptotic process Source: BHF-UCL
  16. negative regulation of neuron death Source: ParkinsonsUK-UCL
  17. negative regulation of protein binding Source: UniProtKB
  18. negative regulation of protein export from nucleus Source: ParkinsonsUK-UCL
  19. negative regulation of protein K48-linked deubiquitination Source: ParkinsonsUK-UCL
  20. negative regulation of protein kinase activity Source: ParkinsonsUK-UCL
  21. negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
  22. negative regulation of ubiquitin-specific protease activity Source: ParkinsonsUK-UCL
  23. oxidation-reduction process Source: GOC
  24. positive regulation of androgen receptor activity Source: ParkinsonsUK-UCL
  25. positive regulation of interleukin-8 production Source: ParkinsonsUK-UCL
  26. positive regulation of oxidative phosphorylation uncoupler activity Source: Ensembl
  27. positive regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
  28. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  29. protein stabilization Source: UniProtKB
  30. regulation of androgen receptor signaling pathway Source: UniProtKB
  31. regulation of inflammatory response Source: UniProtKB
  32. regulation of neuron apoptotic process Source: UniProtKB
  33. single fertilization Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase, Protease

Keywords - Biological processi

Autophagy, Fertilization, Inflammatory response, Stress response

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

SignaLinkiQ99497.

Protein family/group databases

MEROPSiC56.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DJ-1 (EC:3.4.-.-)
Alternative name(s):
Oncogene DJ1
Parkinson disease protein 7
Gene namesi
Name:PARK7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:16369. PARK7.

Subcellular locationi

Cell membrane; Lipid-anchor. Cytoplasm. Nucleus. Membrane raft. Mitochondrion
Note: Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage. Detected in tau inclusions in brains from neurodegenerative disease patients. Membrane raft localization in astrocytes and neuronal cells requires palmitoylation.11 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. membrane raft Source: UniProtKB-SubCell
  5. mitochondrion Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Parkinson disease 7 (PARK7) [MIM:606324]: A neurodegenerative disorder characterized by resting tremor, postural tremor, bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7 has onset before 40 years, slow progression and initial good response to levodopa. Some patients may show traits reminiscent of amyotrophic lateral sclerosis-parkinsonism/dementia complex (Guam disease).
Note: The disease is caused by mutations affecting the gene represented in this entry.8 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 2 Publications
VAR_020492
Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 3 Publications
VAR_020493
Natural varianti104 – 1041A → T in PARK7. 1 Publication
VAR_020495
Natural varianti149 – 1491D → A in PARK7. 1 Publication
Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
VAR_020496
Natural varianti166 – 1661L → P in PARK7; reduces protein stability and leads to increased degradation; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; ubiquitinated by PARK2, leading to its recognition by HDAC6 and targeting to aggresome where is degraded. 5 Publications
Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
VAR_020498

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461C → A: Reduced localization in lipid rafts; when associated with A-106. 4 Publications
Mutagenesisi46 – 461C → A: Reduces protein stability. No effect on oxidation. 4 Publications
Mutagenesisi46 – 461C → S: No effect on mitochondrial translocation. 4 Publications
Mutagenesisi51 – 511V → A: Disrupts dimer formation and strongly reduces ability to eliminate hydrogen peroxide. 1 Publication
Mutagenesisi53 – 531C → A: Strongly reduces chaperone activity and ability to eliminate hydrogen peroxide. 4 Publications
Mutagenesisi53 – 531C → S: No effect on mitochondrial translocation. 4 Publications
Mutagenesisi106 – 1061C → A: Abolishes oxidation, association with mitochondria and protease activity. No effect on chaperone activity. Reduced binding to OTUD7B. 7 Publications
Mutagenesisi106 – 1061C → A: Reduced localization in lipid rafts; when associated with A-46. 7 Publications
Mutagenesisi106 – 1061C → D: Abolishes oxidation and association with mitochondria. No effect on chaperone activity. 7 Publications
Mutagenesisi106 – 1061C → S: No effect on mitochondrial translocation. Reduced protease activity. 7 Publications
Mutagenesisi126 – 1261H → A: Abolishes protease activity. 1 Publication
Mutagenesisi130 – 1301K → R: Partially compensates for loss of stability; when associated with P-166. 1 Publication
Mutagenesisi166 – 1661L → P: Reduced localization in lipid rafts. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism, Tumor suppressor

Organism-specific databases

MIMi168600. phenotype.
606324. phenotype.
Orphaneti90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
2828. Young adult-onset Parkinsonism.
PharmGKBiPA32946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 189Removed in mature formPRO_0000405558
Chaini1 – ?Protein DJ-1PRO_0000157849

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi46 – 461S-palmitoyl cysteine1 Publication
Lipidationi53 – 531S-palmitoyl cysteine1 Publication
Modified residuei67 – 671Phosphotyrosine1 Publication
Modified residuei106 – 1061Cysteine sulfinic acid (-SO2H); alternate
Lipidationi106 – 1061S-palmitoyl cysteine; alternate1 Publication
Cross-linki130 – 130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei148 – 1481N6-acetyllysine By similarity
Modified residuei182 – 1821N6-succinyllysine By similarity

Post-translational modificationi

Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and essential for cell-growth promoting activity and transforming activity.1 Publication
Cys-106 is easily oxidized to sulfinic acid.
Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Oxidation, Palmitate, Phosphoprotein, Ubl conjugation, Zymogen

Proteomic databases

MaxQBiQ99497.
PaxDbiQ99497.
PeptideAtlasiQ99497.
PRIDEiQ99497.

2D gel databases

OGPiQ99497.
REPRODUCTION-2DPAGEIPI00298547.
UCD-2DPAGEO14805.
Q99497.

PTM databases

PhosphoSiteiQ99497.

Miscellaneous databases

PMAP-CutDBQ99497.

Expressioni

Tissue specificityi

Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain. Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa.4 Publications

Inductioni

By hydrogen peroxide and UV irradiation.2 Publications

Gene expression databases

ArrayExpressiQ99497.
BgeeiQ99497.
CleanExiHS_PARK7.
GenevestigatoriQ99497.

Organism-specific databases

HPAiCAB005870.
HPA004190.

Interactioni

Subunit structurei

Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and MTERF.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP102756EBI-1164361,EBI-608057
DAXXQ9UER73EBI-1164361,EBI-77321
FADDQ131589EBI-1164361,EBI-494804
MTA2O947763EBI-1164361,EBI-1783035
OTUD7BQ6GQQ93EBI-1164361,EBI-527784

Protein-protein interaction databases

BioGridi116446. 61 interactions.
DIPiDIP-35515N.
IntActiQ99497. 31 interactions.
MINTiMINT-5003468.
STRINGi9606.ENSP00000340278.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106
Helixi16 – 2813
Beta strandi32 – 376
Turni38 – 414
Beta strandi47 – 493
Beta strandi51 – 533
Beta strandi55 – 573
Helixi58 – 625
Beta strandi68 – 725
Helixi76 – 849
Helixi86 – 9712
Beta strandi101 – 1055
Turni106 – 1083
Helixi109 – 1146
Helixi127 – 1293
Helixi130 – 1334
Turni134 – 1363
Beta strandi139 – 1413
Beta strandi145 – 1495
Beta strandi152 – 1554
Helixi158 – 1603
Helixi161 – 17313
Helixi175 – 1828
Helixi183 – 1853

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J42X-ray2.50A1-189[»]
1P5FX-ray1.10A1-189[»]
1PDVX-ray1.80A1-189[»]
1PDWX-ray2.20A/B/C/D/E/F/G/H1-189[»]
1PE0X-ray1.70A/B1-189[»]
1Q2UX-ray1.60A1-189[»]
1SOAX-ray1.20A1-189[»]
1UCFX-ray1.95A/B1-189[»]
2OR3X-ray1.20A/B1-189[»]
2R1TX-ray1.70A/B2-188[»]
2R1UX-ray1.50A/B2-188[»]
2R1VX-ray1.70A/B2-188[»]
2RK3X-ray1.05A1-189[»]
2RK4X-ray1.15A1-189[»]
2RK6X-ray1.15A1-189[»]
3B36X-ray1.50A1-189[»]
3B38X-ray1.85A1-189[»]
3B3AX-ray1.50A1-189[»]
3BWEX-ray2.40A/B/C/D/E/F/G1-189[»]
3CY6X-ray1.35A1-189[»]
3CYFX-ray1.60A1-189[»]
3CZ9X-ray1.15A1-189[»]
3CZAX-ray1.20A1-189[»]
3EZGX-ray1.15A1-189[»]
3F71X-ray1.20A1-189[»]
3SF8X-ray1.56A/B1-189[»]
4BTEX-ray1.38A1-189[»]
4MNTX-ray1.58A1-189[»]
4MTCX-ray1.47A1-189[»]
4N0MX-ray1.95A1-189[»]
4N12X-ray1.48A1-189[»]
4OQ4X-ray1.49A1-189[»]
4P2GX-ray1.35A1-189[»]
4P34X-ray1.55A1-189[»]
4P35X-ray1.75A1-189[»]
4P36X-ray1.18A1-189[»]
ProteinModelPortaliQ99497.
SMRiQ99497. Positions 3-188.

Miscellaneous databases

EvolutionaryTraceiQ99497.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C56 family.

Phylogenomic databases

eggNOGiCOG0693.
HOGENOMiHOG000063194.
HOVERGENiHBG053511.
InParanoidiQ99497.
KOiK05687.
OMAiGTTFPFA.
OrthoDBiEOG7CVPZX.
PhylomeDBiQ99497.
TreeFamiTF300119.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view]
PfamiPF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01383. not_thiJ. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99497-1 [UniParc]FASTAAdd to Basket

« Hide

MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV    50
VICPDASLED AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG 100
LIAAICAGPT ALLAHEIGFG SKVTTHPLAK DKMMNGGHYT YSENRVEKDG 150
LILTSRGPGT SFEFALAIVE ALNGKEVAAQ VKAPLVLKD 189
Length:189
Mass (Da):19,891
Last modified:July 5, 2004 - v2
Checksum:i4B21661B3A76BC67
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261M → I in PARK7; does not affect protein stability and degradation; does not interfere with homodimerization. 2 Publications
VAR_020492
Natural varianti64 – 641E → D in PARK7; no apparent effect on protein stability; impaired mitochondrial morphology. 3 Publications
VAR_020493
Natural varianti98 – 981R → Q.4 Publications
Corresponds to variant rs71653619 [ dbSNP | Ensembl ].
VAR_020494
Natural varianti104 – 1041A → T in PARK7. 1 Publication
VAR_020495
Natural varianti149 – 1491D → A in PARK7. 1 Publication
Corresponds to variant rs74315352 [ dbSNP | Ensembl ].
VAR_020496
Natural varianti150 – 1501G → S.1 Publication
VAR_020497
Natural varianti163 – 1631E → K.1 Publication
VAR_034801
Natural varianti166 – 1661L → P in PARK7; reduces protein stability and leads to increased degradation; interferes with homodimerization; abolishes interaction with PIAS2; strongly reduces chaperone activity; ubiquitinated by PARK2, leading to its recognition by HDAC6 and targeting to aggresome where is degraded. 5 Publications
Corresponds to variant rs28938172 [ dbSNP | Ensembl ].
VAR_020498
Natural varianti171 – 1711A → S.1 Publication
VAR_020499

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti119 – 1191F → C in BAB71782. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D61380 mRNA. Translation: BAA09603.2.
AF021819 mRNA. Translation: AAC12806.1.
AB073864 mRNA. Translation: BAB71782.1.
AK312000 mRNA. Translation: BAG34938.1.
AL034417 Genomic DNA. Translation: CAB52550.1.
CH471130 Genomic DNA. Translation: EAW71591.1.
BC008188 mRNA. Translation: AAH08188.1.
AB045294 Genomic DNA. No translation available.
AY648999 Genomic DNA. Translation: AAT68961.1.
CCDSiCCDS93.1.
PIRiJC5394.
RefSeqiNP_001116849.1. NM_001123377.1.
NP_009193.2. NM_007262.4.
XP_005263481.1. XM_005263424.1.
UniGeneiHs.419640.

Genome annotation databases

EnsembliENST00000338639; ENSP00000340278; ENSG00000116288.
ENST00000377488; ENSP00000366708; ENSG00000116288.
ENST00000377491; ENSP00000366711; ENSG00000116288.
ENST00000493373; ENSP00000465404; ENSG00000116288.
ENST00000493678; ENSP00000418770; ENSG00000116288.
GeneIDi11315.
KEGGihsa:11315.
UCSCiuc001aou.4. human.

Polymorphism databases

DMDMi56404943.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D61380 mRNA. Translation: BAA09603.2 .
AF021819 mRNA. Translation: AAC12806.1 .
AB073864 mRNA. Translation: BAB71782.1 .
AK312000 mRNA. Translation: BAG34938.1 .
AL034417 Genomic DNA. Translation: CAB52550.1 .
CH471130 Genomic DNA. Translation: EAW71591.1 .
BC008188 mRNA. Translation: AAH08188.1 .
AB045294 Genomic DNA. No translation available.
AY648999 Genomic DNA. Translation: AAT68961.1 .
CCDSi CCDS93.1.
PIRi JC5394.
RefSeqi NP_001116849.1. NM_001123377.1.
NP_009193.2. NM_007262.4.
XP_005263481.1. XM_005263424.1.
UniGenei Hs.419640.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J42 X-ray 2.50 A 1-189 [» ]
1P5F X-ray 1.10 A 1-189 [» ]
1PDV X-ray 1.80 A 1-189 [» ]
1PDW X-ray 2.20 A/B/C/D/E/F/G/H 1-189 [» ]
1PE0 X-ray 1.70 A/B 1-189 [» ]
1Q2U X-ray 1.60 A 1-189 [» ]
1SOA X-ray 1.20 A 1-189 [» ]
1UCF X-ray 1.95 A/B 1-189 [» ]
2OR3 X-ray 1.20 A/B 1-189 [» ]
2R1T X-ray 1.70 A/B 2-188 [» ]
2R1U X-ray 1.50 A/B 2-188 [» ]
2R1V X-ray 1.70 A/B 2-188 [» ]
2RK3 X-ray 1.05 A 1-189 [» ]
2RK4 X-ray 1.15 A 1-189 [» ]
2RK6 X-ray 1.15 A 1-189 [» ]
3B36 X-ray 1.50 A 1-189 [» ]
3B38 X-ray 1.85 A 1-189 [» ]
3B3A X-ray 1.50 A 1-189 [» ]
3BWE X-ray 2.40 A/B/C/D/E/F/G 1-189 [» ]
3CY6 X-ray 1.35 A 1-189 [» ]
3CYF X-ray 1.60 A 1-189 [» ]
3CZ9 X-ray 1.15 A 1-189 [» ]
3CZA X-ray 1.20 A 1-189 [» ]
3EZG X-ray 1.15 A 1-189 [» ]
3F71 X-ray 1.20 A 1-189 [» ]
3SF8 X-ray 1.56 A/B 1-189 [» ]
4BTE X-ray 1.38 A 1-189 [» ]
4MNT X-ray 1.58 A 1-189 [» ]
4MTC X-ray 1.47 A 1-189 [» ]
4N0M X-ray 1.95 A 1-189 [» ]
4N12 X-ray 1.48 A 1-189 [» ]
4OQ4 X-ray 1.49 A 1-189 [» ]
4P2G X-ray 1.35 A 1-189 [» ]
4P34 X-ray 1.55 A 1-189 [» ]
4P35 X-ray 1.75 A 1-189 [» ]
4P36 X-ray 1.18 A 1-189 [» ]
ProteinModelPortali Q99497.
SMRi Q99497. Positions 3-188.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116446. 61 interactions.
DIPi DIP-35515N.
IntActi Q99497. 31 interactions.
MINTi MINT-5003468.
STRINGi 9606.ENSP00000340278.

Protein family/group databases

MEROPSi C56.002.

PTM databases

PhosphoSitei Q99497.

Polymorphism databases

DMDMi 56404943.

2D gel databases

OGPi Q99497.
REPRODUCTION-2DPAGE IPI00298547.
UCD-2DPAGE O14805.
Q99497.

Proteomic databases

MaxQBi Q99497.
PaxDbi Q99497.
PeptideAtlasi Q99497.
PRIDEi Q99497.

Protocols and materials databases

DNASUi 11315.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338639 ; ENSP00000340278 ; ENSG00000116288 .
ENST00000377488 ; ENSP00000366708 ; ENSG00000116288 .
ENST00000377491 ; ENSP00000366711 ; ENSG00000116288 .
ENST00000493373 ; ENSP00000465404 ; ENSG00000116288 .
ENST00000493678 ; ENSP00000418770 ; ENSG00000116288 .
GeneIDi 11315.
KEGGi hsa:11315.
UCSCi uc001aou.4. human.

Organism-specific databases

CTDi 11315.
GeneCardsi GC01P008014.
GeneReviewsi PARK7.
HGNCi HGNC:16369. PARK7.
HPAi CAB005870.
HPA004190.
MIMi 168600. phenotype.
602533. gene.
606324. phenotype.
neXtProti NX_Q99497.
Orphaneti 90020. Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
2828. Young adult-onset Parkinsonism.
PharmGKBi PA32946.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0693.
HOGENOMi HOG000063194.
HOVERGENi HBG053511.
InParanoidi Q99497.
KOi K05687.
OMAi GTTFPFA.
OrthoDBi EOG7CVPZX.
PhylomeDBi Q99497.
TreeFami TF300119.

Enzyme and pathway databases

SignaLinki Q99497.

Miscellaneous databases

EvolutionaryTracei Q99497.
GeneWikii PARK7.
GenomeRNAii 11315.
NextBioi 42983.
PMAP-CutDB Q99497.
PROi Q99497.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q99497.
Bgeei Q99497.
CleanExi HS_PARK7.
Genevestigatori Q99497.

Family and domain databases

Gene3Di 3.40.50.880. 1 hit.
InterProi IPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view ]
Pfami PF01965. DJ-1_PfpI. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
TIGRFAMsi TIGR01383. not_thiJ. 1 hit.
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Publicationsi

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  1. "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras."
    Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K., Iguchi-Ariga S.M.M., Ariga H.
    Biochem. Biophys. Res. Commun. 231:509-513(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Cervix carcinoma.
  2. "Homo sapiens RNA-binding protein regulatory subunit mRNA."
    Beaudoin R., Hod Y.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. "Human DJ-1 cDNA from PC3 cells."
    Ariga H., Niki T.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thalamus.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  8. "Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter."
    Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.
    Gene 263:285-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    Tissue: Kidney.
  9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-27; 33-89; 99-122 AND 149-175, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "DJ-1 gene G150S mutation."
    Zou H.Q., Chan P.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-189, VARIANT SER-150.
  11. "DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor."
    Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M., Ariga H.
    J. Biol. Chem. 276:37556-37563(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, FUNCTION.
  12. "L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system."
    Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R., McLendon C., Carter D.M., Zhu P.-P., Stadler J., Chandran J., Klinefelter G.R., Blackstone C., Cookson M.R.
    J. Biol. Chem. 278:36588-36595(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION BY THE PROTEASOME, SUBCELLULAR LOCATION, INTERACTION WITH PIAS2, HOMODIMERIZATION, MUTAGENESIS OF LYS-130, CHARACTERIZATION OF VARIANT PARK7 PRO-166.
  13. "A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization."
    Moore D.J., Zhang L., Dawson T.M., Dawson V.L.
    J. Neurochem. 87:1558-1567(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION BY THE PROTEASOME, CHARACTERIZATION OF VARIANTS PARK7 ILE-26 AND PRO-166.
  14. "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex."
    Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.
    Mol. Cancer Res. 1:247-261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EFCAB6, FUNCTION.
  15. "Immunocytochemical localization of DJ-1 in human male reproductive tissue."
    Yoshida K., Sato Y., Yoshiike M., Nozawa S., Ariga H., Iwamoto T.
    Mol. Reprod. Dev. 66:391-397(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  16. Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  17. Cited for: TISSUE SPECIFICITY.
  18. "DJ-1 has a role in antioxidative stress to prevent cell death."
    Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H.
    EMBO Rep. 5:213-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, MUTAGENESIS OF VAL-51 AND CYS-53.
  19. "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation."
    Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A.
    PLoS Biol. 2:1-10(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
  20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
    Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H.
    Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
  22. "DJ-1 interacts with HIPK1 and affects H2O2-induced cell death."
    Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M., Ariga H.
    Free Radic. Res. 40:155-165(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-106.
  23. "DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."
    Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.
    Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. Cited for: FUNCTION.
  25. "Mitochondrial localization of DJ-1 leads to enhanced neuroprotection."
    Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M.
    J. Neurosci. Res. 87:123-129(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
  26. "Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage."
    Chen J., Li L., Chin L.S.
    Hum. Mol. Genet. 19:2395-2408(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, MUTAGENESIS OF CYS-106 AND HIS-126.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
    McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
    J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B, MUTAGENESIS OF CYS-106.
  29. "DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."
    Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.
    Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PALMITOYLATION AT CYS-46; CYS-53 AND CYS-106, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-46; CYS-106 AND LEU-166.
  30. "Crystal structure of DJ-1/RS and implication on familial Parkinson's disease."
    Huai Q., Sun Y., Wang H., Chin L.-S., Li L., Robinson H., Ke H.
    FEBS Lett. 549:171-175(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), HOMODIMERIZATION.
  31. "Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease."
    Tao X., Tong L.
    J. Biol. Chem. 278:31372-31379(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130, HOMODIMERIZATION.
  32. "The crystal structure of DJ-1, a protein related to male fertility and Parkinson's disease."
    Honbou K., Suzuki N.N., Horiuchi M., Niki T., Taira T., Ariga H., Inagaki F.
    J. Biol. Chem. 278:31380-31384(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), HOMODIMERIZATION.
  33. "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain."
    Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.
    J. Biol. Chem. 278:44552-44559(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION, HOMODIMERIZATION.
  34. "The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease."
    Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION, LACK OF PROTEOLYTIC ACTIVITY.
  35. "The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization."
    Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C., Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R.
    Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, OXIDATION, FUNCTION, SUBCELLULAR LOCATION.
  36. "The role of pathogenic DJ-1 mutations in Parkinson's disease."
    Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W.
    Ann. Neurol. 54:283-286(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PARK7 ILE-26 AND ALA-149, VARIANT GLN-98.
  37. Cited for: VARIANT PARK7 PRO-166, SUBCELLULAR LOCATION.
  38. Cited for: VARIANT GLN-98.
  39. Cited for: VARIANT PARK7 ASP-64, X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  40. "Differential effects of Parkinson's disease-associated mutations on stability and folding of DJ-1."
    Goerner K., Holtorf E., Odoy S., Nuscher B., Yamamoto A., Regula J.T., Beyer K., Haass C., Kahle P.J.
    J. Biol. Chem. 279:6943-6951(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166.
  41. Cited for: VARIANT PARK7 THR-104, VARIANTS GLN-98 AND SER-171.
  42. Cited for: VARIANT GLN-98.
  43. Cited for: VARIANT LYS-163.
  44. "Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6."
    Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D., Chin L.S.
    J. Cell Biol. 178:1025-1038(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT PARK7 PRO-166.
  45. "Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1."
    Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.
    PLoS ONE 5:E9367-E9367(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASP-64.

Entry informationi

Entry nameiPARK7_HUMAN
AccessioniPrimary (citable) accession number: Q99497
Secondary accession number(s): B2R4Z1
, O14805, Q6DR95, Q7LFU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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